MolNFT v1 · #168504 · protein

Cdib from acinetobacter baumannii

6WIL · Hemolysin activator protein cdib: “Cdib from acinetobacter baumannii”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.87). MolNFT v1 #168504 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6WIL
Type: protein
Length: 536 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemolysin activator protein cdib
UniProt: A0A241YIJ9
Ligands: SO4
Pockets: 3 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hemolysin activator protein cdib	protein	536	15% helix, 51% strand	A0A241YIJ9

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A
C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1165	0.87	0.89	127	empty
2	181	0.66	0.86	40	empty
3	67	0.43	0.81	15	empty

Modifications

Observed in the structure: 6 modified, 1 disulfide (engineered, disulfide).

Compared structures

6WIL · CdiB from Acinetobacter baumannii · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A0A241YIJ9
Elsewhere: RCSB PDB 6WIL · PDBe 6WIL · UniProt A0A241YIJ9

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